NDLI: Kinetic characterization of brush border myosin-I ATPase.

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Kinetic characterization of brush border myosin-I ATPase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Milligan, R. A. Pollard, T. D. Ostap, E. M. Jontes, J. D.
Description	Author Affiliation: Jontes JD ( Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.);
Abstract	Brush border myosin-I (BBM-I) is a single-headed unconventional myosin found in the microvilli of intestinal epithelial cells. We used stopped-flow kinetic analysis to measure the rate and equilibrium constants for several steps in the BBM-I ATPase cycle. We determined the rates for ATP binding to BBM-I and brush border actomyosin-I (actoBBM-I), the rate of actoBBM-I dissociation by ATP, and the rates for the steps in ADP dissociation from actoBBM-I. The rate and equilibrium constants for several of the steps in the actoBBM-I ATPase are significantly different from those of other members of the myosin superfamily. Most notably, dissociation of the actoBBM-I complex by ATP and release of ADP from actoBBM-I are both very slow. The slow rates of these steps may play a role in lengthening the time spent in force-generating states and in limiting the maximal rate of BBM-I motility. In addition, release of ADP from the actoBBM-I complex occurs in at least two steps. This study provides evidence for a member of the myosin superfamily with markedly divergent kinetic behavior.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	26
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Myosins Metabolism Kinetics Chemistry Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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